NOCT_HUMAN
ID NOCT_HUMAN Reviewed; 431 AA.
AC Q9UK39; D3DNY5; Q14D51; Q9HD93; Q9HD94; Q9HD95;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Nocturnin {ECO:0000312|HGNC:HGNC:14254};
DE EC=3.1.3.108 {ECO:0000269|PubMed:31147539};
DE AltName: Full=Carbon catabolite repression 4-like protein;
DE Flags: Precursor;
GN Name=NOCT {ECO:0000312|HGNC:HGNC:14254}; Synonyms=CCR4, CCRN4L, NOC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10521507; DOI=10.1074/jbc.274.43.31068;
RA Dupressoir A., Barbot W., Loireau M.-P., Heidmann T.;
RT "Characterization of a mammalian gene related to the yeast CCR4 general
RT transcription factor and revealed by transposon insertion.";
RL J. Biol. Chem. 274:31068-31075(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 67-431.
RA Wang Y., Osterbur D.L., Green C.B., Besharse J.C.;
RT "Mammalian homologs of Xenopus nocturnin: conservation of structure and
RT circadian regulation.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=22331129; DOI=10.1038/oby.2012.37;
RA Hee S.W., Tsai S.H., Chang Y.C., Chang C.J., Yu I.S., Lee P.C., Lee W.J.,
RA Yun-Chia Chang E., Chuang L.M.;
RT "The role of nocturnin in early adipogenesis and modulation of systemic
RT insulin resistance in human.";
RL Obesity 20:1558-1565(2012).
RN [6]
RP REVIEW.
RX PubMed=22608110; DOI=10.1016/j.tem.2012.03.007;
RA Stubblefield J.J., Terrien J., Green C.B.;
RT "Nocturnin: at the crossroads of clocks and metabolism.";
RL Trends Endocrinol. Metab. 23:326-333(2012).
RN [7] {ECO:0007744|PDB:6BT1, ECO:0007744|PDB:6BT2}
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 120-431 IN COMPLEX WITH
RP MAGNESIUM, FUNCTION, COFACTOR, LACK OF ADENYLASE ACTIVITY, AND MUTAGENESIS
RP OF ASN-149; GLU-195; HIS-286; ASP-324; ASN-326; ASP-377 AND HIS-414.
RX PubMed=29860338; DOI=10.1093/nar/gky412;
RA Abshire E.T., Chasseur J., Bohn J.A., Del Rizzo P.A., Freddolino P.L.,
RA Goldstrohm A.C., Trievel R.C.;
RT "The structure of human Nocturnin reveals a conserved ribonuclease domain
RT that represses target transcript translation and abundance in cells.";
RL Nucleic Acids Res. 46:6257-6270(2018).
RN [8] {ECO:0007744|PDB:6MAL}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 122-431 IN COMPLEX WITH
RP MAGNESIUM, AND LACK OF ADENYLASE ACTIVITY.
RX PubMed=30389976; DOI=10.1038/s41598-018-34615-0;
RA Estrella M.A., Du J., Korennykh A.;
RT "Crystal Structure of Human Nocturnin Catalytic Domain.";
RL Sci. Rep. 8:16294-16294(2018).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 122-431 IN COMPLEX WITH METAL AND
RP NADPH, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-160; GLU-195; LYS-219; HIS-286; LYS-288; ARG-290;
RP LYS-365 AND ARG-367.
RX PubMed=31147539; DOI=10.1038/s41467-019-10125-z;
RA Estrella M.A., Du J., Chen L., Rath S., Prangley E., Chitrakar A., Aoki T.,
RA Schedl P., Rabinowitz J., Korennykh A.;
RT "The metabolites NADP+ and NADPH are the targets of the circadian protein
RT Nocturnin (Curled).";
RL Nat. Commun. 10:2367-2367(2019).
CC -!- FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to
CC NAD(+) and of NADPH to NADH (PubMed:31147539). Shows a small preference
CC for NADPH over NADP(+) (PubMed:31147539). Represses translation and
CC promotes degradation of target mRNA molecules (PubMed:29860338). Plays
CC an important role in post-transcriptional regulation of metabolic genes
CC under circadian control (By similarity). Exerts a rhythmic post-
CC transcriptional control of genes necessary for metabolic functions
CC including nutrient absorption, glucose/insulin sensitivity, lipid
CC metabolism, adipogenesis, inflammation and osteogenesis (By
CC similarity). Plays an important role in favoring adipogenesis over
CC osteoblastogenesis and acts as a key regulator of the
CC adipogenesis/osteogenesis balance (By similarity). Promotes
CC adipogenesis by facilitating PPARG nuclear translocation which
CC activates its transcriptional activity (By similarity). Regulates
CC circadian expression of NOS2 in the liver and negatively regulates the
CC circadian expression of IGF1 in the bone (By similarity). Critical for
CC proper development of early embryos (By similarity).
CC {ECO:0000250|UniProtKB:O35710, ECO:0000269|PubMed:29860338,
CC ECO:0000269|PubMed:31147539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = NAD(+) + phosphate; Xref=Rhea:RHEA:28050,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58349; EC=3.1.3.108;
CC Evidence={ECO:0000269|PubMed:31147539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28051;
CC Evidence={ECO:0000269|PubMed:31147539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADPH = NADH + phosphate; Xref=Rhea:RHEA:60664,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57945; EC=3.1.3.108;
CC Evidence={ECO:0000269|PubMed:31147539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60665;
CC Evidence={ECO:0000269|PubMed:31147539};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:30389976};
CC Note=Binds 2 magnesium ions, but the ions are only loosely bound to the
CC protein. {ECO:0000269|PubMed:29860338};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=173 uM for NADPH {ECO:0000269|PubMed:31147539};
CC -!- SUBUNIT: Interacts with PPARG. {ECO:0000250|UniProtKB:O35710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35710}. Nucleus
CC {ECO:0000250|UniProtKB:O35710}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O35710}. Mitochondrion
CC {ECO:0000269|PubMed:31147539}.
CC -!- TISSUE SPECIFICITY: Adipose tissue. Expression is higher in
CC subcutaneous adipose tissue as compared to visceral adipose tissue.
CC {ECO:0000269|PubMed:22331129}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
CC -!- CAUTION: Was initially shown to have low deadenylase activity that was
CC lost when the metal-binding Glu was mutated (By similarity). Later
CC studies showed that the purified protein lacked deadenylase activity
CC (PubMed:29860338, PubMed:30389976). Was subsequently shown to act as a
CC phosphatase (PubMed:31147539). {ECO:0000250|UniProtKB:O35710,
CC ECO:0000269|PubMed:29860338, ECO:0000269|PubMed:30389976,
CC ECO:0000269|PubMed:31147539}.
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DR EMBL; AF183961; AAD56548.1; -; mRNA.
DR EMBL; CH471056; EAX05129.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX05131.1; -; Genomic_DNA.
DR EMBL; BC113494; AAI13495.1; -; mRNA.
DR EMBL; BC113500; AAI13501.1; -; mRNA.
DR EMBL; AF199492; AAG01387.1; -; Genomic_DNA.
DR EMBL; AF199493; AAG01388.1; -; mRNA.
DR EMBL; AF199494; AAG01389.1; -; Transcribed_RNA.
DR CCDS; CCDS3743.1; -.
DR RefSeq; NP_036250.2; NM_012118.3.
DR PDB; 6BT1; X-ray; 1.48 A; A=120-431.
DR PDB; 6BT2; X-ray; 2.41 A; A/B=120-431.
DR PDB; 6MAL; X-ray; 2.60 A; A=122-431.
DR PDB; 6NF0; X-ray; 2.70 A; A=122-431.
DR PDBsum; 6BT1; -.
DR PDBsum; 6BT2; -.
DR PDBsum; 6MAL; -.
DR PDBsum; 6NF0; -.
DR AlphaFoldDB; Q9UK39; -.
DR SMR; Q9UK39; -.
DR BioGRID; 117347; 74.
DR IntAct; Q9UK39; 28.
DR STRING; 9606.ENSP00000280614; -.
DR iPTMnet; Q9UK39; -.
DR PhosphoSitePlus; Q9UK39; -.
DR BioMuta; NOCT; -.
DR DMDM; 212276446; -.
DR EPD; Q9UK39; -.
DR jPOST; Q9UK39; -.
DR MassIVE; Q9UK39; -.
DR MaxQB; Q9UK39; -.
DR PaxDb; Q9UK39; -.
DR PeptideAtlas; Q9UK39; -.
DR PRIDE; Q9UK39; -.
DR ProteomicsDB; 84714; -.
DR Antibodypedia; 16153; 129 antibodies from 30 providers.
DR DNASU; 25819; -.
DR Ensembl; ENST00000280614.4; ENSP00000280614.2; ENSG00000151014.6.
DR GeneID; 25819; -.
DR KEGG; hsa:25819; -.
DR MANE-Select; ENST00000280614.4; ENSP00000280614.2; NM_012118.4; NP_036250.2.
DR UCSC; uc003ihl.5; human.
DR CTD; 25819; -.
DR DisGeNET; 25819; -.
DR GeneCards; NOCT; -.
DR HGNC; HGNC:14254; NOCT.
DR HPA; ENSG00000151014; Tissue enhanced (bone).
DR MIM; 608468; gene.
DR neXtProt; NX_Q9UK39; -.
DR OpenTargets; ENSG00000151014; -.
DR PharmGKB; PA26176; -.
DR VEuPathDB; HostDB:ENSG00000151014; -.
DR eggNOG; KOG0620; Eukaryota.
DR GeneTree; ENSGT00940000155249; -.
DR HOGENOM; CLU_016428_1_2_1; -.
DR InParanoid; Q9UK39; -.
DR OMA; FRLKRDC; -.
DR OrthoDB; 1387401at2759; -.
DR PhylomeDB; Q9UK39; -.
DR TreeFam; TF323175; -.
DR BioCyc; MetaCyc:ENSG00000151014-MON; -.
DR BRENDA; 3.1.3.108; 2681.
DR PathwayCommons; Q9UK39; -.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR SignaLink; Q9UK39; -.
DR BioGRID-ORCS; 25819; 15 hits in 1067 CRISPR screens.
DR ChiTaRS; NOCT; human.
DR GenomeRNAi; 25819; -.
DR Pharos; Q9UK39; Tbio.
DR PRO; PR:Q9UK39; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UK39; protein.
DR Bgee; ENSG00000151014; Expressed in buccal mucosa cell and 116 other tissues.
DR ExpressionAtlas; Q9UK39; baseline and differential.
DR Genevisible; Q9UK39; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0019178; F:NADP phosphatase activity; IDA:UniProtKB.
DR GO; GO:0102757; F:NADPH phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:Ensembl.
DR GO; GO:0048255; P:mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0006739; P:NADP metabolic process; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0033962; P:P-body assembly; IEA:Ensembl.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0009991; P:response to extracellular stimulus; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR CDD; cd09096; Deadenylase_nocturnin; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR034965; Deadenylase_nocturnin.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR040109; Nocturnin.
DR PANTHER; PTHR12121:SF45; PTHR12121:SF45; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Mitochondrion; Nucleus; Reference proteome; Repressor;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..75
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 76..431
FT /note="Nocturnin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000218568"
FT REGION 20..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..353
FT /note="Interaction with PPARG"
FT /evidence="ECO:0000250|UniProtKB:O35710"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29860338,
FT ECO:0000269|PubMed:30389976, ECO:0000269|PubMed:31147539,
FT ECO:0007744|PDB:6BT1, ECO:0007744|PDB:6BT2,
FT ECO:0007744|PDB:6MAL, ECO:0007744|PDB:6NF0"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31147539"
FT BINDING 219..221
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31147539"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31147539"
FT BINDING 286..289
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31147539"
FT BINDING 324..326
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31147539"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:31147539"
FT VARIANT 140
FT /note="H -> Y (in dbSNP:rs2271777)"
FT /id="VAR_047096"
FT MUTAGEN 149
FT /note="N->A: Slightly decreased activity as transcriptional
FT repressor."
FT /evidence="ECO:0000269|PubMed:29860338"
FT MUTAGEN 160
FT /note="D->A: Lack of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 195
FT /note="E->A: Slightly increased activity as transcriptional
FT repressor. Lack of catalytic activity."
FT /evidence="ECO:0000269|PubMed:29860338,
FT ECO:0000269|PubMed:31147539"
FT MUTAGEN 219
FT /note="K->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 286
FT /note="H->A: No effect on activity as transcriptional
FT repressor."
FT /evidence="ECO:0000269|PubMed:29860338"
FT MUTAGEN 286
FT /note="H->N: Lack of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 288
FT /note="K->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 290
FT /note="R->A: Lack of catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 324
FT /note="D->A: No effect on activity as transcriptional
FT repressor."
FT /evidence="ECO:0000269|PubMed:29860338"
FT MUTAGEN 326
FT /note="N->A: No effect on activity as transcriptional
FT repressor."
FT /evidence="ECO:0000269|PubMed:29860338"
FT MUTAGEN 365
FT /note="K->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 367
FT /note="R->A: Reduced catalytic activity."
FT /evidence="ECO:0000269|PubMed:31147539"
FT MUTAGEN 377
FT /note="D->A: Slightly decreased activity as transcriptional
FT repressor."
FT /evidence="ECO:0000269|PubMed:29860338"
FT MUTAGEN 414
FT /note="H->A,N: Decreased activity as transcriptional
FT repressor."
FT /evidence="ECO:0000269|PubMed:29860338"
FT CONFLICT 16
FT /note="D -> G (in Ref. 1; AAD56548)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="T -> N (in Ref. 4; AAG01387)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> G (in Ref. 1; AAD56548)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> T (in Ref. 4; AAG01389)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> N (in Ref. 1; AAD56548)"
FT /evidence="ECO:0000305"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:6MAL"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:6BT1"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:6BT1"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 245..257
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 260..273
FT /evidence="ECO:0007829|PDB:6BT1"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 294..311
FT /evidence="ECO:0007829|PDB:6BT1"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 347..351
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 377..382
FT /evidence="ECO:0007829|PDB:6BT1"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6BT1"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6BT1"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:6BT2"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:6BT1"
SQ SEQUENCE 431 AA; 48196 MW; 5BDEFC43173B2D0C CRC64;
MFHSPRRLCS ALLQRDAPGL RRLPAPGLRR PLSPPAAVPR PASPRLLAAA SAASGAARSC
SRTVCSMGTG TSRLYSALAK TLNSSAASQH PEYLVSPDPE HLEPIDPKEL LEECRAVLHT
RPPRFQRDFV DLRTDCPSTH PPIRVMQWNI LAQALGEGKD NFVQCPVEAL KWEERKCLIL
EEILAYQPDI LCLQEVDHYF DTFQPLLSRL GYQGTFFPKP WSPCLDVEHN NGPDGCALFF
LQNRFKLVNS ANIRLTAMTL KTNQVAIAQT LECKESGRQF CIAVTHLKAR TGWERFRSAQ
GCDLLQNLQN ITQGAKIPLI VCGDFNAEPT EEVYKHFASS SLNLNSAYKL LSADGQSEPP
YTTWKIRTSG ECRHTLDYIW YSKHALNVRS ALDLLTEEQI GPNRLPSFNY PSDHLSLVCD
FSFTEESDGL S
